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RILP encodes a lysosomal protein that interacts with RAB7, a small GTPase that controls transport to endocytic degradative compartments. Additionally we are shipping RILP Proteins (3) and RILP Kits (2) and many more products for this protein.
Showing 10 out of 13 products:
Human Polyclonal RILP Primary Antibody for IHC - ABIN966968
Cantalupo, Alifano, Roberti, Bruni, Bucci: Rab-interacting lysosomal protein (RILP): the Rab7 effector required for transport to lysosomes. in The EMBO journal 2001
Show all 4 references for ABIN966968
RILP suppresses the invasion of breast cancer cells by interacting with RalGDS (show RALGDS Antibodies) to inhibit its guanine nucleotide exchange factor (show RASGRF1 Antibodies) activity for RalA (show rala Antibodies).
RILP regulates vacuolar ATPase (show DNAH8 Antibodies) through interaction with the V1G1 subunit
VPS41 (show VPS41 Antibodies) subunit of HOPS (show ALPL Antibodies) complex was defined to be the major partner for interacting with RILP.
RILP regulates the activity of the V-ATPase (show ATP6V1H Antibodies) through its interaction with V1G1.
RILP directly and concomitantly binds the tethering HOPS (show ALPL Antibodies) complex and the p150(Glued (show DCTN1 Antibodies)) subunit of the dynein motor. ORP1L then functions as a cholesterol-sensing switch controlling RILP-HOPS (show ALPL Antibodies)-p150(Glued (show DCTN1 Antibodies)) interactions.
Unique region in RILP responsible for its specific role in regulating lysosomal morphology as well as in its interaction with Rab7 (show RAB7B Antibodies) and Rab34 (show RAB34 Antibodies).
The crystal structure of Rab7 (show RAB7B Antibodies)-GTP (show AK3 Antibodies) in complex with the Rab7 (show RAB7B Antibodies) binding domain of RILP reveals that Rab7 (show RAB7B Antibodies) interacts with RILP specifically via two distinct areas.
The data together indicate that RILP, as already demonstrated for several other Rab (show HRB Antibodies) effector proteins, is capable of self-association, thus probably forming a homo-dimer.
RILP indeed prenylated, while phosphorylation analysis showed that the two protein kinase A sites are phosphorylated.
Hence, RILPsv provides an extra dimension to the control of vesicle fusion and transport by the small GTPase (show RACGAP1 Antibodies) Rab7 (show RAB7B Antibodies).
A new mechanism by which the dynein-dynactin (show DCTN1 Antibodies) motor complex recognizes Mreg (show MREG Antibodies) on mature melanosomes is revealed through interaction with RILP and is involved in the centripetal movement of melanosomes.
Rab36 (show RAB36 Antibodies) mediates retrograde melanosome transport in melanocytes through interaction with RILP.
CD63 (show CD63 Antibodies), but not RILP, is recruited to the phagosomes in macrophages expressing the dominant negative form of Rab7 (show RAB7A Antibodies).
This gene encodes a lysosomal protein that interacts with RAB7, a small GTPase that controls transport to endocytic degradative compartments. Studies using mutant forms of the two proteins suggest that this protein represents a downstream effector for RAB7, and both proteins act together in the regulation of late endocytic traffic. A unique region of this protein has also been shown to be involved in the regulation of lysosomal morphology.
Rab interacting lysosomal protein
, rab-interacting lysosomal protein